University of Groningen
Single-molecule fret study on structural dynamics of membrane proteins Aminian Jazi, Atieh
DOI:
10.33612/diss.135802718
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Publication date: 2020
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Aminian Jazi, A. (2020). Single-molecule fret study on structural dynamics of membrane proteins. University of Groningen. https://doi.org/10.33612/diss.135802718
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Propositions accompanying the thesis By Atieh Aminian
Single-Molecule FRET Study on Structural Dynamics of Membrane Proteins
1. Your assumptions are your windows on the world. Scrub them off every once in a while, or the light won't come in. _Isaac Asimov.
2. Null results and failed experiments are still results. Academic communities must change their bias publication preference for positive results. Fails from experimental projects provide deeper, long-term learning insights.
3. Robust and sensitive smFRET dyes are a prerequisite for a reliable translation of information gained in vitro studies to in vivo situation (chapter 2) .
4. SmFRET and X-ray crystallography have proven to be successful to investigate the dynamics and structure of membrane proteins. However, the combination of these methods with most recent techniques such as Cryo-EM can have revolutionary impact to provide further insights into biochemical properties and dynamics of biomolecular systems. 5. BetP senses and rearranges the C-terminal helices in response to increasing
concentration of K+ within an optimal protein/Amphipol complex that potentially could represent the native protein state (chapter 4).
6. SmFRET revelead that the protein in detergent micelles is unable to adopt a fully activated state (chapter4).
7. The ‘caged FRET’ technique is not only suitable for smFRET analysis of complex biochemical systems, but it may also be used to study the intermolecular details of low -affinity binding interactions with diffusion-based smFRET (chapter 3 and perspective).
